Evidence map›Paper›PMID 34019093›Full record

ReviewBrain : a journal of neurology2021

Karyopherin abnormalities in neurodegenerative proteinopathies.

Terouz Pasha, Anna Zatorska, Daulet Sharipov, Boris Rogelj, Tibor Hortobágyi, Frank Hirth

Open access · hybridAbstract readReview
In one paragraph

Review in Brain : a journal of neurology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.5field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. 1-L Transcription in Prion Diseases.International journal of molecular sciences · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  17. Review
  18. Roles of Non-Coding RNA in Alzheimer's Disease Pathophysiology.International journal of molecular sciences · 2023
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 4 countries.

Terouz PashaKing's College London, Institute of Psychiatry, Psychology and Neuroscience, Maurice Wohl Clinical Neuroscience Institute, Department of Basic and Clinical Neuroscience, Institute of Psychiatry, Psychology and Neuroscience, London SE5 9RT, UK.ORCID 0000-0002-5339-8839
Anna ZatorskaKing's College London, Institute of Psychiatry, Psychology and Neuroscience, Maurice Wohl Clinical Neuroscience Institute, Department of Basic and Clinical Neuroscience, Institute of Psychiatry, Psychology and Neuroscience, London SE5 9RT, UK.ORCID 0000-0001-6559-0193
Daulet SharipovKing's College London, Institute of Psychiatry, Psychology and Neuroscience, Maurice Wohl Clinical Neuroscience Institute, Department of Basic and Clinical Neuroscience, Institute of Psychiatry, Psychology and Neuroscience, London SE5 9RT, UK.ORCID 0000-0003-1898-0185
Boris RogeljJozef Stefan Institute, Department of Biotechnology, 1000 Ljubljana, Slovenia.ORCID 0000-0003-3898-1943
Tibor HortobágyiELKH-DE Cerebrovascular and Neurodegenerative Research Group, Department of Neurology, University of Debrecen, 4032 Debrecen, Hungary.ORCID 0000-0001-5732-7942
Frank HirthKing's College London, Institute of Psychiatry, Psychology and Neuroscience, Maurice Wohl Clinical Neuroscience Institute, Department of Basic and Clinical Neuroscience, Institute of Psychiatry, Psychology and Neuroscience, London SE5 9RT, UK.ORCID 0000-0001-8581-9450
King's College London · GBUniversity of Debrecen · HUUniversity of Ljubljana · SI

Funding

REGULATION OF COLLAGENASE 3 GENE EXPRESSION BY CYTOKINESK08AR002012 · NIAMS · MASSACHUSETTS GENERAL HOSPITAL · PI RAHMAN, MAHBOOB U · 1998 to 2002
$374k
Motor Neurone Disease Association HIRTH/OCT13/868-792Motor Neurone Disease Association HIRTH/OCT16/890-792
6 · The paper itself

Abstract

Neurodegenerative proteinopathies are characterized by progressive cell loss that is preceded by the mislocalization and aberrant accumulation of proteins prone to aggregation. Despite their different physiological functions, disease-related proteins like tau, α-synuclein, TAR DNA binding protein-43, fused in sarcoma and mutant huntingtin, all share low complexity regions that can mediate their liquid-liquid phase transitions. The proteins' phase transitions can range from native monomers to soluble oligomers, liquid droplets and further to irreversible, often-mislocalized aggregates that characterize the stages and severity of neurodegenerative diseases. Recent advances into the underlying pathogenic mechanisms have associated mislocalization and aberrant accumulation of disease-related proteins with defective nucleocytoplasmic transport and its mediators called karyopherins. These studies identify karyopherin abnormalities in amyotrophic lateral sclerosis, frontotemporal dementia, Alzheimer's disease, and synucleinopathies including Parkinson's disease and dementia with Lewy bodies, that range from altered expression levels to the subcellular mislocalization and aggregation of karyopherin α and β proteins. The reported findings reveal that in addition to their classical function in nuclear import and export, karyopherins can also act as chaperones by shielding aggregation-prone proteins against misfolding, accumulation and irreversible phase-transition into insoluble aggregates. Karyopherin abnormalities can, therefore, be both the cause and consequence of protein mislocalization and aggregate formation in degenerative proteinopathies. The resulting vicious feedback cycle of karyopherin pathology and proteinopathy identifies karyopherin abnormalities as a common denominator of onset and progression of neurodegenerative disease. Pharmacological targeting of karyopherins, already in clinical trials as therapeutic intervention targeting cancers such as glioblastoma and viral infections like COVID-19, may therefore represent a promising new avenue for disease-modifying treatments in neurodegenerative proteinopathies.

Indexed as

AnimalsBrainHumansKaryopherinsNeurodegenerative DiseasesNeuroprotective AgentsProteostasis DeficienciesKaryopherinsNeuroprotective Agentskaryopherinneurodegenerationnucleocytoplasmic transportphase transitionprotein aggregation

Identifiers

PMID34019093
PMCPMC8194669
OpenAlexW3163921934

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.